(data stored in SCRATCH zone)

SWISSPROT: C0ZLY0_RHOE4

ID   C0ZLY0_RHOE4            Unreviewed;       291 AA.
AC   C0ZLY0;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   RecName: Full=Glucose-1-phosphate thymidylyltransferase {ECO:0000256|RuleBase:RU003706};
DE            EC=2.7.7.24 {ECO:0000256|RuleBase:RU003706};
GN   Name=rmlA {ECO:0000313|EMBL:BAH30957.1};
GN   OrderedLocusNames=RER_02490 {ECO:0000313|EMBL:BAH30957.1};
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH30957.1, ECO:0000313|Proteomes:UP000002204};
RN   [1] {ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAH30957.1, ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX   PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA   Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA   Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA   Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT   "Sequence analysis of three plasmids harboured in Rhodococcus
RT   erythropolis strain PR4.";
RL   Environ. Microbiol. 8:334-346(2006).
CC   -!- FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and
CC       glucose 1-phosphate, as well as its pyrophosphorolysis.
CC       {ECO:0000256|RuleBase:RU003706}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate +
CC         dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477,
CC         ChEBI:CHEBI:58601; EC=2.7.7.24;
CC         Evidence={ECO:0000256|RuleBase:RU003706};
CC   -!- SIMILARITY: Belongs to the glucose-1-phosphate
CC       thymidylyltransferase family. {ECO:0000256|RuleBase:RU003706}.
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DR   EMBL; AP008957; BAH30957.1; -; Genomic_DNA.
DR   RefSeq; WP_020905793.1; NC_012490.1.
DR   STRING; 234621.RER_02490; -.
DR   EnsemblBacteria; BAH30957; BAH30957; RER_02490.
DR   KEGG; rer:RER_02490; -.
DR   PATRIC; fig|234621.6.peg.683; -.
DR   eggNOG; ENOG4107QPT; Bacteria.
DR   eggNOG; COG1209; LUCA.
DR   HOGENOM; HOG000283473; -.
DR   KO; K00973; -.
DR   OMA; KPSWRNE; -.
DR   Proteomes; UP000002204; Chromosome.
DR   GO; GO:0008879; F:glucose-1-phosphate thymidylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
DR   CDD; cd02538; G1P_TT_short; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR005907; G1P_thy_trans_s.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR43532; PTHR43532; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR01207; rmlA; 1.
PE   3: Inferred from homology;
DR   PRODOM; C0ZLY0.
DR   SWISS-2DPAGE; C0ZLY0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002204};
KW   Magnesium {ECO:0000256|RuleBase:RU003706};
KW   Metal-binding {ECO:0000256|RuleBase:RU003706};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU003706,
KW   ECO:0000313|EMBL:BAH30957.1};
KW   Transferase {ECO:0000256|RuleBase:RU003706,
KW   ECO:0000313|EMBL:BAH30957.1}.
FT   DOMAIN        3    236       NTP_transferase. {ECO:0000259|Pfam:
FT                                PF00483}.
SQ   SEQUENCE   291 AA;  32096 MW;  D8AAC52CC53BF0A1 CRC64;
     MRGIILAGGT GSRLHPITLG VSKQLVPVYD KPMIYYPLST LMLAGIRDIM IITTEDDAPQ
     FQRLLGDGSQ FGVDLTYQIQ HEPNGLAQAF VLGAGHIGSE SAALVLGDNI FYGPGLGSKL
     TRFENIDGGA VFAYWVSDPT AYGVIEFDRE GKAVSLEEKP ANPRSNYSVP GLYFYDNDVV
     AIAKDLEPSA RGEYEITDVN RAYLEAGRLQ VEVLPRGTAW LDTGTFDSLL DASNYVRTIE
     ERQGLKIGAP EEVAWRHGFI TDDELRIRAE KLLKSGYGKY LLELLDRGKD W
//

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